Phospholipase C-gamma: diverse roles in receptor-mediated calcium signaling

Trends Biochem Sci. 2005 Dec;30(12):688-97. doi: 10.1016/j.tibs.2005.10.005. Epub 2005 Nov 2.


Ca2+ is a universal signal: the dynamic changes in its release and entry trigger a plethora of cellular responses. Central to this schema are members of the phospholipase C (PLC) superfamily, which relay information from the activated receptor to downstream signal cascades by production of second-messenger molecules. Recent studies reveal that, in addition to its enzymatic activity, PLC-gamma regulates Ca2+ entry via the formation of an intermolecular lipid-binding domain with canonical transient receptor potential 3 (TRPC3) ion channels. This complex, in turn, controls TRPC3 trafficking and cell-surface expression. Thus, TRPC3 ion channels are functionally linked to both lipase-dependent and -independent activities of PLC-gamma. Understanding the underlying molecular mechanisms that regulate this complex will probably clarify the processes of receptor-activated Ca2+ entry.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites / genetics
  • Calcium Signaling*
  • Evolution, Molecular
  • Humans
  • Models, Biological
  • Models, Molecular
  • Molecular Sequence Data
  • Phospholipase C gamma / chemistry
  • Phospholipase C gamma / genetics
  • Phospholipase C gamma / metabolism*
  • Protein Conformation
  • Protein Structure, Tertiary
  • Sequence Homology, Amino Acid
  • TRPC Cation Channels / chemistry
  • TRPC Cation Channels / genetics
  • TRPC Cation Channels / metabolism


  • TRPC Cation Channels
  • TRPC3 cation channel
  • Phospholipase C gamma